Affinity-purified Phaseolus vulgaris lectin (PHA-E) is a tetrameric glycoprotein responsible for the erythroagglutinating properties of the PHA fraction. It has carbohydrate specificity for oligosaccharides and elutes with bovine thyroglobulin or acetic acid. PHA-E binds to human erythrocytes and lymphocytes, with a preference for blood group A (-SA), and lymphocytes have five times more PHA-E receptors than erythrocytes. The crystal structure of ligand-free PHA-E features a typical legume lectin fold with two β-sheets and two α-helices, containing one GlcNAc residue from the N-linked glycan. An asparagine-linked glycopeptide inhibits PHA-E-induced agglutination and mitogenicity. PHA-E binds di-galactosylated and bisected N-glycans, making it useful for detecting bisecting GlcNAc- and Gal-bearing glycoproteins.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

mmunohistochemistry, Immunocytochemistry, Immunofluorescence study, Bioconjugations, Blotting, Cell typing, HNK1 binding study, Glycobiology.

References

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